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Database: PDB
Entry: 4I51
LinkDB: 4I51
Original site: 4I51 
HEADER    TRANSFERASE/PEPTIDE                     28-NOV-12   4I51              
TITLE     METHYLTRANSFERASE DOMAIN OF HUMAN EUCHROMATIC HISTONE                 
TITLE    2 METHYLTRANSFERASE 1, MUTANT Y1211A                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE EHMT1;                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: EUCHROMATIC HISTONE-LYSINE N-METHYLTRANSFERASE 1, EU-       
COMPND   5 HMTASE1, G9A-LIKE PROTEIN 1, GLP, GLP1, HISTONE H3-K9                
COMPND   6 METHYLTRANSFERASE 5, H3-K9-HMTASE 5, LYSINE N-METHYLTRANSFERASE 1D;  
COMPND   7 EC: 2.1.1.-, 2.1.1.43;                                               
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES;                                                       
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: H3K9 NE-ALLYL PEPTIDE;                                     
COMPND  12 CHAIN: C, D;                                                         
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: UNKNOWN PEPTIDE;                                           
COMPND  16 CHAIN: K;                                                            
COMPND  17 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: EHMT1, EUHMTASE1, GLP, KIAA1876, KMT1D;                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21-V2R-PRARE2;                           
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28-LIC;                                
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606;                                                
SOURCE  16 MOL_ID: 3;                                                           
SOURCE  17 SYNTHETIC: YES                                                       
KEYWDS    NE-ALLYL PEPTIDE, STRUCTURAL GENOMICS CONSORTIUM, TRANSFERASE-PEPTIDE 
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.DONG,H.ZENG,J.R.WALKER,K.ISLAM,C.BOUNTRA,C.H.ARROWSMITH,            
AUTHOR   2 A.M.EDWARDS,M.LOU,J.MIN,H.WU,STRUCTURAL GENOMICS CONSORTIUM (SGC)    
REVDAT   3   02-APR-14 4I51    1       SOURCE                                   
REVDAT   2   04-DEC-13 4I51    1       JRNL                                     
REVDAT   1   19-DEC-12 4I51    0                                                
SPRSDE     19-DEC-12 4I51      4H4H                                             
JRNL        AUTH   K.ISLAM,Y.CHEN,H.WU,I.R.BOTHWELL,G.J.BLUM,H.ZENG,A.DONG,     
JRNL        AUTH 2 W.ZHENG,J.MIN,H.DENG,M.LUO                                   
JRNL        TITL   DEFINING EFFICIENT ENZYME-COFACTOR PAIRS FOR BIOORTHOGONAL   
JRNL        TITL 2 PROFILING OF PROTEIN METHYLATION.                            
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 110 16778 2013              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   24082136                                                     
JRNL        DOI    10.1073/PNAS.1216365110                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0027,COOT 0.6                             
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.78                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 52354                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.171                           
REMARK   3   R VALUE            (WORKING SET) : 0.171                           
REMARK   3   FREE R VALUE                     : 0.195                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1075                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3194                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 84.04                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2710                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 59                           
REMARK   3   BIN FREE R VALUE                    : 0.2770                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4298                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 87                                      
REMARK   3   SOLVENT ATOMS            : 503                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.11                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.55000                                              
REMARK   3    B22 (A**2) : 0.37000                                              
REMARK   3    B33 (A**2) : -0.91000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.130         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.117         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.082         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.250         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.953                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4538 ; 0.008 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6162 ; 1.163 ; 1.962       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   561 ; 6.945 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   231 ;31.682 ;22.727       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   727 ;13.347 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    51 ;16.898 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   647 ; 0.095 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3575 ; 0.011 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   975        A  1235                          
REMARK   3    RESIDUE RANGE :   A  3001        A  3015                          
REMARK   3    RESIDUE RANGE :   A  3101        A  3378                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.6560  -0.6850 -34.3280              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0167 T22:   0.0410                                     
REMARK   3      T33:   0.0524 T12:  -0.0062                                     
REMARK   3      T13:   0.0142 T23:   0.0017                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7642 L22:   1.3904                                     
REMARK   3      L33:   1.6057 L12:  -0.3427                                     
REMARK   3      L13:  -0.6357 L23:   0.2667                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0177 S12:   0.1112 S13:  -0.0978                       
REMARK   3      S21:   0.0726 S22:  -0.0092 S23:   0.2656                       
REMARK   3      S31:   0.0505 S32:  -0.2534 S33:   0.0269                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   973        B  1235                          
REMARK   3    RESIDUE RANGE :   B  3001        B  3007                          
REMARK   3    RESIDUE RANGE :   B  3101        B  3320                          
REMARK   3    ORIGIN FOR THE GROUP (A):  30.9920   6.6430 -33.2770              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0319 T22:   0.0978                                     
REMARK   3      T33:   0.0806 T12:  -0.0313                                     
REMARK   3      T13:   0.0122 T23:   0.0111                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8212 L22:   1.8017                                     
REMARK   3      L33:   2.6385 L12:   0.6262                                     
REMARK   3      L13:  -0.7205 L23:  -0.0554                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0405 S12:   0.0370 S13:  -0.0712                       
REMARK   3      S21:  -0.0782 S22:   0.0033 S23:  -0.3732                       
REMARK   3      S31:  -0.1379 S32:   0.4594 S33:   0.0371                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   4                                                                      
REMARK   4 4I51 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-DEC-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB076312.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-MAR-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97958                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 52417                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 7.900                              
REMARK 200  R MERGE                    (I) : 0.07200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.93                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 83.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.56100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3HNA                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.28                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% ISOPROPANOL, 20% PEG4000; 0.1M       
REMARK 280  HEPES PH7.5, VAPOR DIFFUSION HANGING DROP, TEMPERATURE 297K         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       41.74850            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       47.52600            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.90000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       47.52600            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       41.74850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.90000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5950 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23650 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B, D, K                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   950                                                      
REMARK 465     ASN A   951                                                      
REMARK 465     SER A   952                                                      
REMARK 465     GLN A   953                                                      
REMARK 465     VAL A   954                                                      
REMARK 465     TRP A   955                                                      
REMARK 465     SER A   956                                                      
REMARK 465     ALA A   957                                                      
REMARK 465     LEU A   958                                                      
REMARK 465     GLN A   959                                                      
REMARK 465     MET A   960                                                      
REMARK 465     SER A   961                                                      
REMARK 465     LYS A   962                                                      
REMARK 465     ALA A   963                                                      
REMARK 465     LEU A   964                                                      
REMARK 465     GLN A   965                                                      
REMARK 465     ASP A   966                                                      
REMARK 465     SER A   967                                                      
REMARK 465     ALA A   968                                                      
REMARK 465     PRO A   969                                                      
REMARK 465     ASP A   970                                                      
REMARK 465     ARG A   971                                                      
REMARK 465     PRO A   972                                                      
REMARK 465     SER A   973                                                      
REMARK 465     PRO A   974                                                      
REMARK 465     GLY B   950                                                      
REMARK 465     ASN B   951                                                      
REMARK 465     SER B   952                                                      
REMARK 465     GLN B   953                                                      
REMARK 465     VAL B   954                                                      
REMARK 465     TRP B   955                                                      
REMARK 465     SER B   956                                                      
REMARK 465     ALA B   957                                                      
REMARK 465     LEU B   958                                                      
REMARK 465     GLN B   959                                                      
REMARK 465     MET B   960                                                      
REMARK 465     SER B   961                                                      
REMARK 465     LYS B   962                                                      
REMARK 465     ALA B   963                                                      
REMARK 465     LEU B   964                                                      
REMARK 465     GLN B   965                                                      
REMARK 465     ASP B   966                                                      
REMARK 465     SER B   967                                                      
REMARK 465     ALA B   968                                                      
REMARK 465     PRO B   969                                                      
REMARK 465     ASP B   970                                                      
REMARK 465     ARG B   971                                                      
REMARK 465     PRO B   972                                                      
REMARK 465     ASN B  1148                                                      
REMARK 465     LYS B  1149                                                      
REMARK 465     ASP B  1150                                                      
REMARK 465     GLY B  1151                                                      
REMARK 465     GLU B  1152                                                      
REMARK 465     THR D  2003                                                      
REMARK 465     LYS D  2004                                                      
REMARK 465     UNK K  1956                                                      
REMARK 465     UNK K  1957                                                      
REMARK 465     UNK K  1958                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A1103    NE   CZ   NH1  NH2                                  
REMARK 470     ARG A1214    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A1221    CE   NZ                                             
REMARK 470     THR C2003    OG1  CG2                                            
REMARK 470     THR C2011    OG1  CG2                                            
REMARK 470     ARG B 981    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS B1055    CG   CD   CE   NZ                                   
REMARK 470     GLU B1067    CD   OE1  OE2                                       
REMARK 470     ARG B1103    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B1104    CG   OD1  OD2                                       
REMARK 470     GLU B1138    CG   CD   OE1  OE2                                  
REMARK 470     ARG B1214    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B1226    CZ   NH1  NH2                                       
REMARK 470     LYS B1231    CD   CE   NZ                                        
REMARK 470     GLN D2005    CG   CD   OE1  NE2                                  
REMARK 470     SER D2010    OG                                                  
REMARK 470     THR D2011    OG1  CG2                                            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 982      106.58   -164.56                                   
REMARK 500    THR A1016      -86.35   -100.69                                   
REMARK 500    ASP A1035     -147.84   -116.63                                   
REMARK 500    MET A1049      -58.17     78.12                                   
REMARK 500    ASN A1086       50.27    -95.18                                   
REMARK 500    VAL A1088      -64.30   -138.88                                   
REMARK 500    ASN A1163     -161.13   -105.25                                   
REMARK 500    MET A1183      -92.37   -125.93                                   
REMARK 500    ALA A1203      124.89    -35.21                                   
REMARK 500    ASP B 982      107.82   -163.95                                   
REMARK 500    VAL B 998      -56.97   -127.62                                   
REMARK 500    ASP B 999     -159.81   -142.14                                   
REMARK 500    SER B1005       24.14   -144.72                                   
REMARK 500    ASN B1006       31.82    -82.70                                   
REMARK 500    THR B1016      -90.47    -98.88                                   
REMARK 500    ASP B1035     -148.98   -125.72                                   
REMARK 500    MET B1049      -53.01     73.06                                   
REMARK 500    ASN B1086       51.64    -95.39                                   
REMARK 500    VAL B1088      -56.36   -135.87                                   
REMARK 500    VAL B1121      -60.17    -99.36                                   
REMARK 500    ASN B1163     -159.75   -110.01                                   
REMARK 500    GLU B1173       70.23   -117.32                                   
REMARK 500    MET B1183      -90.47   -134.20                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B3003  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1037   SG                                                     
REMARK 620 2 CYS B1084   SG  112.2                                              
REMARK 620 3 CYS B1080   SG  106.9 113.7                                        
REMARK 620 4 CYS B1074   SG  111.0 106.1 107.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A3003  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1084   SG                                                     
REMARK 620 2 CYS A1037   SG  113.6                                              
REMARK 620 3 CYS A1080   SG  112.4 106.3                                        
REMARK 620 4 CYS A1074   SG  107.2 110.3 106.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B3004  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1033   SG                                                     
REMARK 620 2 CYS B1042   SG  106.5                                              
REMARK 620 3 CYS B1031   SG  107.4 111.2                                        
REMARK 620 4 CYS B1037   SG  110.9 115.8 104.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B3005  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1172   SG                                                     
REMARK 620 2 CYS B1232   SG  101.9                                              
REMARK 620 3 CYS B1225   SG  118.3 108.8                                        
REMARK 620 4 CYS B1227   SG  106.9 116.9 104.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A3005  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1232   SG                                                     
REMARK 620 2 CYS A1172   SG  104.8                                              
REMARK 620 3 CYS A1225   SG  110.1 114.1                                        
REMARK 620 4 CYS A1227   SG  114.6 106.4 107.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B3002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1078   SG                                                     
REMARK 620 2 CYS B1044   SG   97.2                                              
REMARK 620 3 CYS B1074   SG  118.2 112.4                                        
REMARK 620 4 CYS B1031   SG  106.3 116.0 106.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A3004  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1042   SG                                                     
REMARK 620 2 CYS A1031   SG  110.3                                              
REMARK 620 3 CYS A1033   SG  106.2 107.3                                        
REMARK 620 4 CYS A1037   SG  119.4 105.1 108.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A3002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1074   SG                                                     
REMARK 620 2 CYS A1078   SG  118.1                                              
REMARK 620 3 CYS A1044   SG  114.2  97.8                                        
REMARK 620 4 CYS A1031   SG  106.7 106.8 113.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH A 3001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 3002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 3003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 3004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 3005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 3006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 3007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH B 3001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 3002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 3003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 3004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 3005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 3006                
DBREF  4I51 A  951  1235  UNP    Q9H9B1   EHMT1_HUMAN    982   1266             
DBREF  4I51 B  951  1235  UNP    Q9H9B1   EHMT1_HUMAN    982   1266             
DBREF  4I51 C 2003  2011  PDB    4I51     4I51          2003   2011             
DBREF  4I51 D 2003  2011  PDB    4I51     4I51          2003   2011             
DBREF  4I51 K 1952  1967  PDB    4I51     4I51          1952   1967             
SEQADV 4I51 GLY A  950  UNP  Q9H9B1              EXPRESSION TAG                 
SEQADV 4I51 ALA A 1211  UNP  Q9H9B1    TYR  1242 ENGINEERED MUTATION            
SEQADV 4I51 GLY B  950  UNP  Q9H9B1              EXPRESSION TAG                 
SEQADV 4I51 ALA B 1211  UNP  Q9H9B1    TYR  1242 ENGINEERED MUTATION            
SEQRES   1 A  286  GLY ASN SER GLN VAL TRP SER ALA LEU GLN MET SER LYS          
SEQRES   2 A  286  ALA LEU GLN ASP SER ALA PRO ASP ARG PRO SER PRO VAL          
SEQRES   3 A  286  GLU ARG ILE VAL SER ARG ASP ILE ALA ARG GLY TYR GLU          
SEQRES   4 A  286  ARG ILE PRO ILE PRO CYS VAL ASN ALA VAL ASP SER GLU          
SEQRES   5 A  286  PRO CYS PRO SER ASN TYR LYS TYR VAL SER GLN ASN CYS          
SEQRES   6 A  286  VAL THR SER PRO MET ASN ILE ASP ARG ASN ILE THR HIS          
SEQRES   7 A  286  LEU GLN TYR CYS VAL CYS ILE ASP ASP CYS SER SER SER          
SEQRES   8 A  286  ASN CYS MET CYS GLY GLN LEU SER MET ARG CYS TRP TYR          
SEQRES   9 A  286  ASP LYS ASP GLY ARG LEU LEU PRO GLU PHE ASN MET ALA          
SEQRES  10 A  286  GLU PRO PRO LEU ILE PHE GLU CYS ASN HIS ALA CYS SER          
SEQRES  11 A  286  CYS TRP ARG ASN CYS ARG ASN ARG VAL VAL GLN ASN GLY          
SEQRES  12 A  286  LEU ARG ALA ARG LEU GLN LEU TYR ARG THR ARG ASP MET          
SEQRES  13 A  286  GLY TRP GLY VAL ARG SER LEU GLN ASP ILE PRO PRO GLY          
SEQRES  14 A  286  THR PHE VAL CYS GLU TYR VAL GLY GLU LEU ILE SER ASP          
SEQRES  15 A  286  SER GLU ALA ASP VAL ARG GLU GLU ASP SER TYR LEU PHE          
SEQRES  16 A  286  ASP LEU ASP ASN LYS ASP GLY GLU VAL TYR CYS ILE ASP          
SEQRES  17 A  286  ALA ARG PHE TYR GLY ASN VAL SER ARG PHE ILE ASN HIS          
SEQRES  18 A  286  HIS CYS GLU PRO ASN LEU VAL PRO VAL ARG VAL PHE MET          
SEQRES  19 A  286  ALA HIS GLN ASP LEU ARG PHE PRO ARG ILE ALA PHE PHE          
SEQRES  20 A  286  SER THR ARG LEU ILE GLU ALA GLY GLU GLN LEU GLY PHE          
SEQRES  21 A  286  ASP ALA GLY GLU ARG PHE TRP ASP ILE LYS GLY LYS LEU          
SEQRES  22 A  286  PHE SER CYS ARG CYS GLY SER PRO LYS CYS ARG HIS SER          
SEQRES   1 C    9  THR LYS GLN THR ALA ARG LDH SER THR                          
SEQRES   1 B  286  GLY ASN SER GLN VAL TRP SER ALA LEU GLN MET SER LYS          
SEQRES   2 B  286  ALA LEU GLN ASP SER ALA PRO ASP ARG PRO SER PRO VAL          
SEQRES   3 B  286  GLU ARG ILE VAL SER ARG ASP ILE ALA ARG GLY TYR GLU          
SEQRES   4 B  286  ARG ILE PRO ILE PRO CYS VAL ASN ALA VAL ASP SER GLU          
SEQRES   5 B  286  PRO CYS PRO SER ASN TYR LYS TYR VAL SER GLN ASN CYS          
SEQRES   6 B  286  VAL THR SER PRO MET ASN ILE ASP ARG ASN ILE THR HIS          
SEQRES   7 B  286  LEU GLN TYR CYS VAL CYS ILE ASP ASP CYS SER SER SER          
SEQRES   8 B  286  ASN CYS MET CYS GLY GLN LEU SER MET ARG CYS TRP TYR          
SEQRES   9 B  286  ASP LYS ASP GLY ARG LEU LEU PRO GLU PHE ASN MET ALA          
SEQRES  10 B  286  GLU PRO PRO LEU ILE PHE GLU CYS ASN HIS ALA CYS SER          
SEQRES  11 B  286  CYS TRP ARG ASN CYS ARG ASN ARG VAL VAL GLN ASN GLY          
SEQRES  12 B  286  LEU ARG ALA ARG LEU GLN LEU TYR ARG THR ARG ASP MET          
SEQRES  13 B  286  GLY TRP GLY VAL ARG SER LEU GLN ASP ILE PRO PRO GLY          
SEQRES  14 B  286  THR PHE VAL CYS GLU TYR VAL GLY GLU LEU ILE SER ASP          
SEQRES  15 B  286  SER GLU ALA ASP VAL ARG GLU GLU ASP SER TYR LEU PHE          
SEQRES  16 B  286  ASP LEU ASP ASN LYS ASP GLY GLU VAL TYR CYS ILE ASP          
SEQRES  17 B  286  ALA ARG PHE TYR GLY ASN VAL SER ARG PHE ILE ASN HIS          
SEQRES  18 B  286  HIS CYS GLU PRO ASN LEU VAL PRO VAL ARG VAL PHE MET          
SEQRES  19 B  286  ALA HIS GLN ASP LEU ARG PHE PRO ARG ILE ALA PHE PHE          
SEQRES  20 B  286  SER THR ARG LEU ILE GLU ALA GLY GLU GLN LEU GLY PHE          
SEQRES  21 B  286  ASP ALA GLY GLU ARG PHE TRP ASP ILE LYS GLY LYS LEU          
SEQRES  22 B  286  PHE SER CYS ARG CYS GLY SER PRO LYS CYS ARG HIS SER          
SEQRES   1 D    9  THR LYS GLN THR ALA ARG LDH SER THR                          
SEQRES   1 K   13  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
MODRES 4I51 LDH C 2009  LYS  N~6~-ETHYL-L-LYSINE                                
MODRES 4I51 LDH D 2009  LYS  N~6~-ETHYL-L-LYSINE                                
HET    LDH  C2009      11                                                       
HET    LDH  D2009      11                                                       
HET    SAH  A3001      26                                                       
HET     ZN  A3002       1                                                       
HET     ZN  A3003       1                                                       
HET     ZN  A3004       1                                                       
HET     ZN  A3005       1                                                       
HET    GOL  A3006       6                                                       
HET    GOL  A3007       6                                                       
HET    UNX  A3008       1                                                       
HET    UNX  A3009       1                                                       
HET    UNX  A3010       1                                                       
HET    UNX  A3011       1                                                       
HET    UNX  A3012       1                                                       
HET    UNX  A3013       1                                                       
HET    UNX  A3014       1                                                       
HET    UNX  A3015       1                                                       
HET    SAH  B3001      26                                                       
HET     ZN  B3002       1                                                       
HET     ZN  B3003       1                                                       
HET     ZN  B3004       1                                                       
HET     ZN  B3005       1                                                       
HET    GOL  B3006       6                                                       
HET    UNX  B3007       1                                                       
HETNAM     LDH N~6~-ETHYL-L-LYSINE                                              
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
HETNAM      ZN ZINC ION                                                         
HETNAM     GOL GLYCEROL                                                         
HETNAM     UNX UNKNOWN ATOM OR ION                                              
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  LDH    2(C8 H18 N2 O2)                                              
FORMUL   6  SAH    2(C14 H20 N6 O5 S)                                           
FORMUL   7   ZN    8(ZN 2+)                                                     
FORMUL  11  GOL    3(C3 H8 O3)                                                  
FORMUL  13  UNX    9(X)                                                         
FORMUL  28  HOH   *503(H2 O)                                                    
HELIX    1   1 ASN A 1024  LEU A 1028  5                                   5    
HELIX    2   2 CYS A 1042  SER A 1048  1                                   7    
HELIX    3   3 VAL A 1088  GLY A 1092  5                                   5    
HELIX    4   4 ASP A 1131  ASP A 1135  1                                   5    
HELIX    5   5 VAL A 1164  ILE A 1168  5                                   5    
HELIX    6   6 GLY A 1212  GLY A 1220  1                                   9    
HELIX    7   7 ASN B 1024  LEU B 1028  5                                   5    
HELIX    8   8 CYS B 1042  SER B 1048  1                                   7    
HELIX    9   9 VAL B 1088  GLY B 1092  5                                   5    
HELIX   10  10 ASP B 1131  ARG B 1137  1                                   7    
HELIX   11  11 VAL B 1164  ILE B 1168  5                                   5    
HELIX   12  12 GLY B 1212  GLY B 1220  1                                   9    
HELIX   13  13 UNK K 1960  UNK K 1967  1                                   5    
SHEET    1   A 4 ARG A 977  SER A 980  0                                        
SHEET    2   A 4 CYS A 994  ASN A 996 -1  O  ASN A 996   N  ARG A 977           
SHEET    3   A 4 LEU A1097  ARG A1101  1  O  LEU A1099   N  VAL A 995           
SHEET    4   A 4 TRP A1107  SER A1111 -1  O  GLY A1108   N  TYR A1100           
SHEET    1   B 4 LYS A1008  TYR A1009  0                                        
SHEET    2   B 4 TYR A1154  GLY A1162  1  O  PHE A1160   N  LYS A1008           
SHEET    3   B 4 GLY A1126  SER A1130 -1  N  GLU A1127   O  ASP A1157           
SHEET    4   B 4 CYS A1014  VAL A1015  1  N  CYS A1014   O  LEU A1128           
SHEET    1   C 4 LYS A1008  TYR A1009  0                                        
SHEET    2   C 4 TYR A1154  GLY A1162  1  O  PHE A1160   N  LYS A1008           
SHEET    3   C 4 LEU A1143  ASP A1145 -1  N  PHE A1144   O  ILE A1156           
SHEET    4   C 4 LDH C2009  SER C2010  1  O  LDH C2009   N  LEU A1143           
SHEET    1   D 4 ILE A1071  PHE A1072  0                                        
SHEET    2   D 4 LEU A1176  PHE A1182  1  O  ARG A1180   N  ILE A1071           
SHEET    3   D 4 ARG A1192  SER A1197 -1  O  ALA A1194   N  VAL A1179           
SHEET    4   D 4 PHE A1120  TYR A1124 -1  N  VAL A1121   O  PHE A1195           
SHEET    1   E 2 ASN A1169  HIS A1170  0                                        
SHEET    2   E 2 GLY A1208  PHE A1209  1  O  PHE A1209   N  ASN A1169           
SHEET    1   F 4 ARG B 977  SER B 980  0                                        
SHEET    2   F 4 CYS B 994  ASN B 996 -1  O  CYS B 994   N  VAL B 979           
SHEET    3   F 4 LEU B1097  ARG B1101  1  O  LEU B1099   N  VAL B 995           
SHEET    4   F 4 TRP B1107  SER B1111 -1  O  ARG B1110   N  GLN B1098           
SHEET    1   G 3 LYS B1008  TYR B1009  0                                        
SHEET    2   G 3 TYR B1154  GLY B1162  1  O  PHE B1160   N  LYS B1008           
SHEET    3   G 3 GLY B1126  SER B1130 -1  N  GLU B1127   O  ASP B1157           
SHEET    1   H 3 LYS B1008  TYR B1009  0                                        
SHEET    2   H 3 TYR B1154  GLY B1162  1  O  PHE B1160   N  LYS B1008           
SHEET    3   H 3 LEU B1143  ASP B1145 -1  N  PHE B1144   O  ILE B1156           
SHEET    1   I 4 ILE B1071  PHE B1072  0                                        
SHEET    2   I 4 LEU B1176  PHE B1182  1  O  PHE B1182   N  ILE B1071           
SHEET    3   I 4 ARG B1192  SER B1197 -1  O  ALA B1194   N  VAL B1179           
SHEET    4   I 4 PHE B1120  TYR B1124 -1  N  VAL B1121   O  PHE B1195           
SHEET    1   J 2 ASN B1169  HIS B1170  0                                        
SHEET    2   J 2 GLY B1208  PHE B1209  1  O  PHE B1209   N  ASN B1169           
LINK         C   LDH C2009                 N   SER C2010     1555   1555  1.33  
LINK         C   LDH D2009                 N   SER D2010     1555   1555  1.33  
LINK         SG  CYS B1037                ZN    ZN B3003     1555   1555  2.24  
LINK         SG  CYS A1084                ZN    ZN A3003     1555   1555  2.26  
LINK         SG  CYS B1033                ZN    ZN B3004     1555   1555  2.26  
LINK         SG  CYS B1172                ZN    ZN B3005     1555   1555  2.28  
LINK         SG  CYS A1232                ZN    ZN A3005     1555   1555  2.29  
LINK         SG  CYS B1232                ZN    ZN B3005     1555   1555  2.30  
LINK         SG  CYS B1084                ZN    ZN B3003     1555   1555  2.30  
LINK         SG  CYS A1037                ZN    ZN A3003     1555   1555  2.30  
LINK         SG  CYS B1078                ZN    ZN B3002     1555   1555  2.31  
LINK         SG  CYS A1042                ZN    ZN A3004     1555   1555  2.31  
LINK         SG  CYS A1080                ZN    ZN A3003     1555   1555  2.31  
LINK         SG  CYS A1031                ZN    ZN A3004     1555   1555  2.32  
LINK         SG  CYS A1074                ZN    ZN A3002     1555   1555  2.32  
LINK         SG  CYS B1044                ZN    ZN B3002     1555   1555  2.32  
LINK         SG  CYS A1078                ZN    ZN A3002     1555   1555  2.33  
LINK         SG  CYS B1042                ZN    ZN B3004     1555   1555  2.33  
LINK         SG  CYS A1074                ZN    ZN A3003     1555   1555  2.33  
LINK         SG  CYS A1172                ZN    ZN A3005     1555   1555  2.34  
LINK         SG  CYS B1080                ZN    ZN B3003     1555   1555  2.34  
LINK         SG  CYS A1033                ZN    ZN A3004     1555   1555  2.34  
LINK         SG  CYS B1031                ZN    ZN B3004     1555   1555  2.34  
LINK         SG  CYS B1074                ZN    ZN B3003     1555   1555  2.35  
LINK         SG  CYS B1074                ZN    ZN B3002     1555   1555  2.35  
LINK         SG  CYS A1044                ZN    ZN A3002     1555   1555  2.36  
LINK         SG  CYS A1225                ZN    ZN A3005     1555   1555  2.36  
LINK         SG  CYS A1037                ZN    ZN A3004     1555   1555  2.37  
LINK         SG  CYS B1037                ZN    ZN B3004     1555   1555  2.37  
LINK         SG  CYS B1225                ZN    ZN B3005     1555   1555  2.38  
LINK         SG  CYS B1031                ZN    ZN B3002     1555   1555  2.42  
LINK         SG  CYS A1227                ZN    ZN A3005     1555   1555  2.42  
LINK         SG  CYS A1031                ZN    ZN A3002     1555   1555  2.44  
LINK         SG  CYS B1227                ZN    ZN B3005     1555   1555  2.66  
SITE     1 AC1 20 MET A1105  GLY A1106  TRP A1107  SER A1141                    
SITE     2 AC1 20 TYR A1142  ARG A1166  PHE A1167  ILE A1168                    
SITE     3 AC1 20 ASN A1169  HIS A1170  PHE A1215  LYS A1219                    
SITE     4 AC1 20 PHE A1223  CYS A1225  ARG A1226  HOH A3151                    
SITE     5 AC1 20 HOH A3173  HOH A3215  HOH A3314  LDH C2009                    
SITE     1 AC2  4 CYS A1031  CYS A1044  CYS A1074  CYS A1078                    
SITE     1 AC3  4 CYS A1037  CYS A1074  CYS A1080  CYS A1084                    
SITE     1 AC4  4 CYS A1031  CYS A1033  CYS A1037  CYS A1042                    
SITE     1 AC5  4 CYS A1172  CYS A1225  CYS A1227  CYS A1232                    
SITE     1 AC6  4 ASN A1013  ILE A1021  ARG A1023  HOH B3266                    
SITE     1 AC7  9 CYS A1033  ILE A1034  ASP A1035  SER A1039                    
SITE     2 AC7  9 ASN A1041  HOH A3365  LEU B1047  LEU B1070                    
SITE     3 AC7  9 PHE B1072                                                     
SITE     1 AC8 14 MET B1105  GLY B1106  TRP B1107  SER B1141                    
SITE     2 AC8 14 TYR B1142  ARG B1166  PHE B1167  ASN B1169                    
SITE     3 AC8 14 HIS B1170  PHE B1223  CYS B1225  ARG B1226                    
SITE     4 AC8 14 HOH B3206  LDH D2009                                          
SITE     1 AC9  4 CYS B1031  CYS B1044  CYS B1074  CYS B1078                    
SITE     1 BC1  4 CYS B1037  CYS B1074  CYS B1080  CYS B1084                    
SITE     1 BC2  4 CYS B1031  CYS B1033  CYS B1037  CYS B1042                    
SITE     1 BC3  4 CYS B1172  CYS B1225  CYS B1227  CYS B1232                    
SITE     1 BC4  5 ARG A1023  HOH A3123  ARG B1023  LEU B1128                    
SITE     2 BC4  5 HOH B3155                                                     
CRYST1   83.497   83.800   95.052  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011976  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011933  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010521        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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